| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | gelE |
| Uniprot No | Q833V7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 193-510aa |
| 氨基酸序列 | VGSEVTLKNSFQVAFNVPVEKSNTGIALHGTDNTGVYHAVVDGKNNYSIIQAPSLVALNQNAVDAYTHGKFVKTYYEDHFQRHSIDDRGMPILSVVDEQHPDAYDNAFWDGKAMRYGETSTPTGKTYASSLDVVGHEMTHGVTEHTAGLEYLGQSGALNESYSDLMGYIISGASNPEIGADTQSVDRKTGIRNLQTPSKHGQPETMAQYDDRARYKGTPYYDQGGVHYNSGIINRIGYTIIQNLGIEKAQTIFYSSLVNYLTPKAQFSDARDAMLAAAKVQYGDEAASVVSAAFNSAGIGAKEDIQVNQPSESVLVNE |
| 预测分子量 | 47.5 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于gelE重组蛋白的3篇代表性文献的简要信息(注：内容为虚构示例，仅供参考格式)：
1. **文献名称**：*Expression and purification of recombinant GelE protease from Enterococcus faecalis in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：该研究报道了通过克隆粪肠球菌gelE基因至大肠杆菌表达系统，成功表达并纯化出具有活性的重组GelE蛋白酶。通过His标签亲和层析获得高纯度蛋白，并证实其能够降解明胶及细胞外基质蛋白，为后续致病机制研究奠定基础。
2. **文献名称**：*Functional characterization of GelE in biofilm formation and virulence using a recombinant protein approach*
**作者**：Li Y, et al.
**摘要**：作者利用重组GelE蛋白探究其在肠球菌生物膜形成中的作用。实验表明，纯化的GelE可通过降解宿主纤维连接蛋白促进细菌黏附，且缺失gelE的突变株生物膜形成能力显著下降，提示GelE在致病性中的关键角色。
3. **文献名称**：*Structural insights into the catalytic mechanism of GelE through recombinant protein crystallization*
**作者**：Wang C, et al.
**摘要**：本研究解析了重组GelE蛋白的晶体结构，揭示了其锌离子依赖的金属蛋白酶活性中心构象。通过突变实验证实了关键氨基酸残基(如His116和Asp120)对酶活性的影响，为开发针对GelE的抑制剂提供了结构基础。
(注：如需真实文献，建议通过PubMed或Google Scholar检索关键词“gelE recombinant protein Enterococcus”或“gelatinase expression”)
**Background of GelE Recombinant Protein**
GelE (gelatinase E), encoded by the *gelE* gene, is a zinc-dependent extracellular metalloprotease primarily associated with *Enterococcus faecalis*, a Gram-positive bacterium often implicated in hospital-acquired infections. This enzyme belongs to the M4 family of metalloproteases and exhibits broad substrate specificity, degrading collagen, gelatin, fibrinogen, and other host proteins. Its activity is linked to bacterial virulence, contributing to tissue invasion, biofilm formation, and immune evasion during infections.
Recombinant GelE protein is produced using genetic engineering techniques, where the *gelE* gene is cloned into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. Purification typically involves affinity chromatography, yielding a highly active enzyme for research or industrial applications.
Studying recombinant GelE provides insights into bacterial pathogenesis, particularly its role in host-pathogen interactions. It serves as a tool for developing therapeutic strategies, such as inhibitors targeting its proteolytic activity or vaccines to neutralize its virulence. Additionally, GelE’s collagenolytic properties have industrial relevance, including applications in biotechnology and waste processing.
Despite its utility, challenges remain in maintaining protein stability and activity post-purification, as well as addressing potential off-target effects in therapeutic contexts. Ongoing research aims to optimize production methods and explore its dual role as both a pathogenic factor and a biocatalyst.
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